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- PDB-4r3o: Human Constitutive 20S Proteasome -

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Basic information

Entry
Database: PDB / ID: 4r3o
TitleHuman Constitutive 20S Proteasome
Components
  • (Proteasome subunit alpha type- ...) x 7
  • (Proteasome subunit beta type- ...) x 7
KeywordsHYDROLASE
Function / homology
Function and homology information


purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding / proteasome endopeptidase complex ...purine ribonucleoside triphosphate binding / regulation of endopeptidase activity / proteasome core complex / Regulation of ornithine decarboxylase (ODC) / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / immune system process / myofibril / NF-kappaB binding / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / negative regulation of inflammatory response to antigenic stimulus / response to organonitrogen compound / proteolysis involved in protein catabolic process / proteasome complex / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / ciliary basal body / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Degradation of DVL / proteasomal protein catabolic process / P-body / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / Degradation of AXIN / lipopolysaccharide binding / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Defective CFTR causes cystic fibrosis / Hedgehog ligand biogenesis / Negative regulation of NOTCH4 signaling / G2/M Checkpoints / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / response to virus / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / ABC-family proteins mediated transport / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / response to organic cyclic compound / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / nuclear matrix / FCERI mediated NF-kB activation / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / UCH proteinases / The role of GTSE1 in G2/M progression after G2 checkpoint / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / Neddylation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / positive regulation of NF-kappaB transcription factor activity / peptidase activity / ER-Phagosome pathway / regulation of inflammatory response / postsynapse / proteasome-mediated ubiquitin-dependent protein catabolic process / secretory granule lumen / endopeptidase activity / response to oxidative stress / ficolin-1-rich granule lumen / nuclear body / ribosome / Ub-specific processing proteases / cadherin binding / intracellular membrane-bounded organelle / centrosome / synapse / ubiquitin protein ligase binding / Neutrophil degranulation / mitochondrion / proteolysis
Similarity search - Function
Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 ...Proteasome subunit alpha 1 / Aminohydrolase, N-terminal nucleophile (Ntn) domain / Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 / Proteasome beta subunit, C-terminal / Proteasome beta subunits C terminal / Proteasome subunit beta 4 / Proteasome subunit beta 2 / Proteasome beta 3 subunit / Proteasome subunit alpha6 / Proteasome subunit alpha5 / Proteasome beta-type subunits signature. / Peptidase T1A, proteasome beta-subunit / Proteasome beta-type subunit, conserved site / Proteasome subunit A N-terminal signature / Proteasome alpha-type subunits signature. / Proteasome alpha-subunit, N-terminal domain / Proteasome subunit A N-terminal signature Add an annotation / Proteasome alpha-type subunit / Proteasome alpha-type subunit profile. / Proteasome B-type subunit / Proteasome beta-type subunit profile. / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 / Proteasome subunit beta type-5 ...Proteasome subunit alpha type-7 / Proteasome subunit beta type-1 / Proteasome subunit alpha type-1 / Proteasome subunit alpha type-2 / Proteasome subunit alpha type-3 / Proteasome subunit alpha type-4 / Proteasome subunit alpha type-5 / Proteasome subunit beta type-4 / Proteasome subunit beta type-6 / Proteasome subunit beta type-5 / Proteasome subunit beta type-3 / Proteasome subunit beta type-2 / Proteasome subunit alpha type-6 / Proteasome subunit beta type-7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsSacchettini, J.C. / Harshbarger, W.H.
CitationJournal: Structure / Year: 2015
Title: Crystal Structure of the Human 20S Proteasome in Complex with Carfilzomib.
Authors: Harshbarger, W. / Miller, C. / Diedrich, C. / Sacchettini, J.
History
DepositionAug 16, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 28, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 4, 2015Group: Database references
Revision 1.2Feb 18, 2015Group: Database references
Revision 1.3Feb 28, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Proteasome subunit alpha type-6
B: Proteasome subunit alpha type-2
C: Proteasome subunit alpha type-4
D: Proteasome subunit alpha type-7
E: Proteasome subunit alpha type-5
F: Proteasome subunit alpha type-1
G: Proteasome subunit alpha type-3
H: Proteasome subunit beta type-6
I: Proteasome subunit beta type-7
J: Proteasome subunit beta type-3
K: Proteasome subunit beta type-2
L: Proteasome subunit beta type-5
M: Proteasome subunit beta type-1
N: Proteasome subunit beta type-4
O: Proteasome subunit alpha type-6
P: Proteasome subunit alpha type-2
Q: Proteasome subunit alpha type-4
R: Proteasome subunit alpha type-7
S: Proteasome subunit alpha type-5
T: Proteasome subunit alpha type-1
U: Proteasome subunit alpha type-3
V: Proteasome subunit beta type-6
W: Proteasome subunit beta type-7
X: Proteasome subunit beta type-3
Y: Proteasome subunit beta type-2
Z: Proteasome subunit beta type-5
1: Proteasome subunit beta type-1
2: Proteasome subunit beta type-4


Theoretical massNumber of molelcules
Total (without water)697,89728
Polymers697,89728
Non-polymers00
Water3,333185
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area110820 Å2
ΔGint-394 kcal/mol
Surface area214650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.227, 205.061, 163.128
Angle α, β, γ (deg.)90.00, 106.37, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25
16
26
17
27
18
28
19
29
110
210
111
211
112
212
113
213
114
214

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'C' and (resseq 2:251 )
211chain 'Q' and (resseq 2:251 )
112chain 'G' and (resseq 1:245 )
212chain 'U' and (resseq 1:245 )
113chain 'A' and (resseq 2:245 )
213chain 'O' and (resseq 2:245 )
114chain 'D' and (resseq 2:244 )
214chain 'R' and (resseq 2:244 )
115chain 'F' and (resseq 4:240 )
215chain 'T' and (resseq 4:240 )
116chain 'E' and (resseq 8:241 )
216chain 'S' and (resseq 8:241 )
117chain 'B' and (resseq 1:233 )
217chain 'P' and (resseq 1:233 )
118chain 'I' and (resseq 1:220 )
218chain 'W' and (resseq 1:220 )
119chain 'N' and (resseq 1:217 )
219chain '2' and (resseq 1:217 )
1110chain 'M' and (resseq 1:213 )
2110chain '1' and (resseq 1:213 )
1111chain 'J' and (resseq 2:205 )
2111chain 'X' and (resseq 2:205 )
1112chain 'H' and (resseq 1:202 )
2112chain 'V' and (resseq 1:202 )
1113chain 'L' and (resseq 1:201 )
2113chain 'Z' and (resseq 1:201 )
1114chain 'K' and (resseq 1:199 )
2114chain 'Y' and (resseq 1:199 )

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

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Components

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Proteasome subunit alpha type- ... , 7 types, 14 molecules AOBPCQDRESFTGU

#1: Protein Proteasome subunit alpha type-6 / / 27 kDa prosomal protein / PROS-27 / p27K / Macropain iota chain / Multicatalytic endopeptidase ...27 kDa prosomal protein / PROS-27 / p27K / Macropain iota chain / Multicatalytic endopeptidase complex iota chain / Proteasome iota chain


Mass: 27186.174 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P60900, proteasome endopeptidase complex
#2: Protein Proteasome subunit alpha type-2 / / Macropain subunit C3 / Multicatalytic endopeptidase complex subunit C3 / Proteasome component C3


Mass: 25796.338 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P25787, proteasome endopeptidase complex
#3: Protein Proteasome subunit alpha type-4 / / Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / ...Macropain subunit C9 / Multicatalytic endopeptidase complex subunit C9 / Proteasome component C9 / Proteasome subunit L


Mass: 28118.189 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-251 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P25789, proteasome endopeptidase complex
#4: Protein Proteasome subunit alpha type-7 / / Proteasome subunit RC6-1 / Proteasome subunit XAPC7


Mass: 27382.178 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-244 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: O14818, proteasome endopeptidase complex
#5: Protein Proteasome subunit alpha type-5 / / Macropain zeta chain / Multicatalytic endopeptidase complex zeta chain / Proteasome zeta chain


Mass: 25569.957 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 8-241 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P28066, proteasome endopeptidase complex
#6: Protein Proteasome subunit alpha type-1 / / 30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex ...30 kDa prosomal protein / PROS-30 / Macropain subunit C2 / Multicatalytic endopeptidase complex subunit C2 / Proteasome component C2 / Proteasome nu chain


Mass: 26728.428 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 4-241 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P25786, proteasome endopeptidase complex
#7: Protein Proteasome subunit alpha type-3 / / Macropain subunit C8 / Multicatalytic endopeptidase complex subunit C8 / Proteasome component C8


Mass: 27287.100 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2-246 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P25788, proteasome endopeptidase complex

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Proteasome subunit beta type- ... , 7 types, 14 molecules HVIWJXKYLZM1N2

#8: Protein Proteasome subunit beta type-6 / / Macropain delta chain / Multicatalytic endopeptidase complex delta chain / Proteasome delta chain / ...Macropain delta chain / Multicatalytic endopeptidase complex delta chain / Proteasome delta chain / Proteasome subunit Y


Mass: 21656.527 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 35-236 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P28072, proteasome endopeptidase complex
#9: Protein Proteasome subunit beta type-7 / / Macropain chain Z / Multicatalytic endopeptidase complex chain Z / Proteasome subunit Z


Mass: 23745.256 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 44-263 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: Q99436, proteasome endopeptidase complex
#10: Protein Proteasome subunit beta type-3 / PSMB3 / Proteasome chain 13 / Proteasome component C10-II / Proteasome theta chain


Mass: 22841.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P49720, proteasome endopeptidase complex
#11: Protein Proteasome subunit beta type-2 / PSMB2 / Macropain subunit C7-I / Multicatalytic endopeptidase complex subunit C7-I / Proteasome component C7-I


Mass: 22720.146 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-199 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P49721, proteasome endopeptidase complex
#12: Protein Proteasome subunit beta type-5 / PSMB5 / Macropain epsilon chain / Multicatalytic endopeptidase complex epsilon chain / Proteasome chain 6 / ...Macropain epsilon chain / Multicatalytic endopeptidase complex epsilon chain / Proteasome chain 6 / Proteasome epsilon chain / Proteasome subunit MB1 / Proteasome subunit X


Mass: 22199.072 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 60-260 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P28074, proteasome endopeptidase complex
#13: Protein Proteasome subunit beta type-1 / PSMB1 / Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / ...Macropain subunit C5 / Multicatalytic endopeptidase complex subunit C5 / Proteasome component C5 / Proteasome gamma chain


Mass: 23578.986 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 29-241 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P20618, proteasome endopeptidase complex
#14: Protein Proteasome subunit beta type-4 / PSMB4 / 26 kDa prosomal protein / HsBPROS26 / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase ...26 kDa prosomal protein / HsBPROS26 / PROS-26 / Macropain beta chain / Multicatalytic endopeptidase complex beta chain / Proteasome beta chain / Proteasome chain 3 / HsN3


Mass: 24138.453 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 46-262 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: red blood cells
References: UniProt: P28070, proteasome endopeptidase complex

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Non-polymers , 1 types, 185 molecules

#15: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 185 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.74 Å3/Da / Density % sol: 55.13 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 40% MPD, 0.2M sodium formate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 120 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97946 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 1, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 2.6→50 Å / Num. all: 228370 / Num. obs: 228052 / % possible obs: 98.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.069
Reflection shellResolution: 2.6→2.64 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.566 / Mean I/σ(I) obs: 2.1 / % possible all: 91.8

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.2_1309)refinement
HKL-3000data collection
HKL-3000data reduction
SCALEPACKdata scaling
PHENIX1.8.2_1309phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→36.339 Å / SU ML: 0.34 / σ(F): 1.34 / Phase error: 29.68 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2442 10249 5.02 %Random
Rwork0.2045 ---
obs0.2065 228052 98.13 %-
all-228370 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.6→36.339 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms47646 0 0 185 47831
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00348544
X-RAY DIFFRACTIONf_angle_d0.77165778
X-RAY DIFFRACTIONf_dihedral_angle_d12.29317499
X-RAY DIFFRACTIONf_chiral_restr0.0537468
X-RAY DIFFRACTIONf_plane_restr0.0038545
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11C1909X-RAY DIFFRACTIONPOSITIONAL
12Q1909X-RAY DIFFRACTIONPOSITIONAL0.008
21G1885X-RAY DIFFRACTIONPOSITIONAL
22U1885X-RAY DIFFRACTIONPOSITIONAL0.008
31A1842X-RAY DIFFRACTIONPOSITIONAL
32O1842X-RAY DIFFRACTIONPOSITIONAL0.008
41D1682X-RAY DIFFRACTIONPOSITIONAL
42R1682X-RAY DIFFRACTIONPOSITIONAL0.009
51F1845X-RAY DIFFRACTIONPOSITIONAL
52T1845X-RAY DIFFRACTIONPOSITIONAL0.032
61E1758X-RAY DIFFRACTIONPOSITIONAL
62S1758X-RAY DIFFRACTIONPOSITIONAL0.009
71B1707X-RAY DIFFRACTIONPOSITIONAL
72P1707X-RAY DIFFRACTIONPOSITIONAL0.018
81I1643X-RAY DIFFRACTIONPOSITIONAL
82W1643X-RAY DIFFRACTIONPOSITIONAL0.01
91N1672X-RAY DIFFRACTIONPOSITIONAL
9221672X-RAY DIFFRACTIONPOSITIONAL0.01
101M1641X-RAY DIFFRACTIONPOSITIONAL
10211641X-RAY DIFFRACTIONPOSITIONAL0.011
111J1585X-RAY DIFFRACTIONPOSITIONAL
112X1585X-RAY DIFFRACTIONPOSITIONAL0.011
121H1509X-RAY DIFFRACTIONPOSITIONAL
122V1509X-RAY DIFFRACTIONPOSITIONAL0.034
131L1548X-RAY DIFFRACTIONPOSITIONAL
132Z1548X-RAY DIFFRACTIONPOSITIONAL0.034
141K1570X-RAY DIFFRACTIONPOSITIONAL
142Y1570X-RAY DIFFRACTIONPOSITIONAL0.009
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.62040.37793360.34625754X-RAY DIFFRACTION79
2.6204-2.65130.4033780.33957118X-RAY DIFFRACTION97
2.6513-2.68360.37843890.33037174X-RAY DIFFRACTION98
2.6836-2.71750.37063580.31537332X-RAY DIFFRACTION99
2.7175-2.75330.35663640.31957303X-RAY DIFFRACTION99
2.7533-2.7910.35863860.30597327X-RAY DIFFRACTION99
2.791-2.83090.30963990.28957289X-RAY DIFFRACTION100
2.8309-2.87310.3193730.27217292X-RAY DIFFRACTION100
2.8731-2.9180.31623980.26677380X-RAY DIFFRACTION100
2.918-2.96580.34823860.27197326X-RAY DIFFRACTION100
2.9658-3.01690.31723900.26037274X-RAY DIFFRACTION100
3.0169-3.07170.30263720.25437388X-RAY DIFFRACTION100
3.0717-3.13080.30844230.2517287X-RAY DIFFRACTION100
3.1308-3.19470.29913940.24577326X-RAY DIFFRACTION100
3.1947-3.26410.2944040.2347322X-RAY DIFFRACTION100
3.2641-3.340.27413580.22597330X-RAY DIFFRACTION100
3.34-3.42340.25243960.20867345X-RAY DIFFRACTION100
3.4234-3.51590.2573930.2027290X-RAY DIFFRACTION100
3.5159-3.61930.2523910.19547375X-RAY DIFFRACTION100
3.6193-3.7360.22473720.19267324X-RAY DIFFRACTION100
3.736-3.86940.23273710.18787332X-RAY DIFFRACTION99
3.8694-4.02410.2483910.18167295X-RAY DIFFRACTION99
4.0241-4.2070.2043680.17017302X-RAY DIFFRACTION99
4.207-4.42840.20364060.1647261X-RAY DIFFRACTION99
4.4284-4.70530.18923780.15667184X-RAY DIFFRACTION98
4.7053-5.06780.18433670.15857233X-RAY DIFFRACTION98
5.0678-5.57610.20313910.17947320X-RAY DIFFRACTION99
5.5761-6.37920.23853700.20167364X-RAY DIFFRACTION99
6.3792-8.02290.20223850.17717271X-RAY DIFFRACTION98
8.0229-36.3430.17773500.16336497X-RAY DIFFRACTION87
Refinement TLS params.Method: refined / Origin x: 150.3744 Å / Origin y: -40.6626 Å / Origin z: 4.539 Å
111213212223313233
T0.2171 Å2-0.026 Å2-0.0235 Å2-0.1621 Å20.0366 Å2--0.2639 Å2
L0.4377 °20.0185 °2-0.1086 °2-0.1408 °2-0.0633 °2--0.4669 °2
S-0.0168 Å °-0.0134 Å °0.0941 Å °-0.019 Å °-0.0136 Å °-0.0192 Å °0.0741 Å °0.0086 Å °-0.0008 Å °
Refinement TLS groupSelection details: all

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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